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Published on July 10, 2003; 10.1104/pp.103.022699

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Received February 25, 2003
Returned for revision April 18, 2003
Accepted May 10, 2003

Interallelic Complementation at the Ubiquitous Urease Coding Locus of Soybean

Ariel Goldraij , Lesa J. Beamer , and Joe C. Polacco *

Department of Biochemistry (A.G., L.J.B., J.C.P.) and Interdisciplinary Plant Group (A.G., J.C.P.), University of Missouri, Columbia, Missouri 65211

* Corresponding author; email: PolaccoJ{at}missouri.edu.

Soybean (Glycine max [L.] Merrill) mutant aj6 carries a single recessive lesion, aj6, that eliminates ubiquitous urease activity in leaves and callus while retaining normal embryo-specific urease activity. Consistently, aj6/aj6 plants accumulated urea in leaves. In crosses of aj6/aj6 by urease mutants at the Eu1, Eu2, and Eu3 loci, F1 individuals exhibited wild-type leaf urease activity, and the F2 segregated urease-negative individuals, demonstrating that aj6 is not an allele at these loci. F2 of aj6/aj6 crossed with a null mutant lacking the Eu1-encoded embryo-specific urease showed that ubiquitous urease was also inactive in seeds of aj6/aj6. The cross of aj6/aj6 to eu4/eu4, a mutant previously assigned to the ubiquitous urease structural gene (R.S. Torisky, J.D. Griffin, R.L. Yenofsky, J.C. Polacco [1994] Mol Gen Genet 242: 404-414), yielded an F1 having 22% ± 11% of wild-type leaf urease activity. Coding sequences for ubiquitous urease were cloned by reverse transcriptase-polymerase chain reaction from wild-type, aj6/aj6, and eu4/eu4 leaf RNA. The ubiquitous urease had an 837-amino acid open reading frame (ORF), 87% identical to the embryo-specific urease. The aj6/aj6 ORF showed an R201C change that cosegregated with the lack of leaf urease activity in a cross against a urease-positive line, whereas the eu4/eu4 ORF showed a G468E change. Heteroallelic interaction in F2 progeny of aj6/aj6 x eu4/eu4 resulted in partially restored leaf urease activity. These results confirm that aj6/aj6 and eu4/eu4 are mutants affected in the ubiquitous urease structural gene. They also indicate that radical amino acid changes in distinct domains can be partially compensated in the urease heterotrimer.




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